@article{THESIS,
      recid = {1353},
      author = {Gong, Zhiliang},
      title = {Membrane Selectivity of Phosphatidylserine Recognizing  Proteins},
      publisher = {University of Chicago},
      school = {Ph.D.},
      address = {2017-06},
      number = {THESIS},
      pages = {131},
      abstract = {The work presented in this thesis is an effort to gain a  more holistic understanding of physicochemical regulators  that drive the membrane selectivity of proteins that  recognize phosphatidylserine (PS). To date, more than forty  PS-binding proteins have been identified [1, 2, 3];  however, what has been largely lacking is the general  approach for describing and understanding PS/protein  interaction in the membrane context. While the importance  of various physicochemical properties of lipid membranes in  protein/lipid interactions has been more progressively  recognized since the proposal of the fluid mosaic model in  the early 1970s [4], most studies in the field have focused  on one or two aspects of the lipid membrane, unable to  account for the important synergistic effects arising from  multiple factors. Strides in resolving the structure of  membrane binding proteins in solution or in crystal have  enabled molecular-level description of protein-lipid  interactions; however, these studies tend to focus on local  chemical identities at the expense of general membrane  properties and their effects on protein structural  arrangement.

The work presented here clearly demonstrate  the necessity of considering both the physical and chemical  properties of the membrane in understanding lipid-protein  interactions. In doing so, a generalizable approach for  understanding lipid-protein interactions has emerged.  First, the interaction configuration of the membrane-bound  protein is proposed by combining molecular dynamics  simulations with experimental methods such as x-ray  reflectivity from lipid monolayers with proteins adsorbed.  Then the lipid-protein interaction is decomposed into  various possible interactions components, such as  electrostatic and hydrophobic interactions, which are then  probed using biochemical assays by varying relevant  physical and chemical parameters as possible modulators for  the membrane selectivity of the protein. The newly  identified interaction components are treated as new  dimensions in the parameter space that determines the  lipid-protein interaction. Lastly, possible interplay and  synergetic effects among the previously known and added  parameters are further examined for a holistic view of the  possible behavior of the protein within the parameter  space.},
      url = {http://knowledge.uchicago.edu/record/1353},
      doi = {https://doi.org/10.6082/uchicago.1353},
}